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Basic Insight on Plant Defensins

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Basic Insight on Plant Defensins Basic insight on plant defensins @ Roxana Portieles, Camilo Ayra, Orlando Borrás Plant Division, Center for Genetic Engineering and Biotechnology, CIGB Ave 31 / 158 and 190, Playa, PO Box 6162, Havana 10 600, Cuba E-mail: [email protected] ABSTRACT REVIEW Defensins are small cysteine-rich peptides with antimicrobial activity. Plant defensins have a characteristic three- dimensional folding pattern that is stabilized by eight disulfide-linked cysteines. This pattern is very similar to defense peptides of mammals and insects, suggesting an ancient and conserved origin. Functionally, these proteins exhibit a diverse array of biological activities, although they all serve a common function as defenders of their hosts. Plant defensins are active against a broad range of phytopathogenic fungi and even against human pathogens, which indicates their potential in therapeutics. This review briefly describes the distribution, structure, function and putative modes of antimicrobial activity of plant defensins and reflects their potential in agriculture and medical applications. Key works: defensin, cysteine-rich peptides, mode of action Biotecnología Aplicada 2006;23:75-78 RESUMEN Conocimientos básicos acerca de las defensinas de plantas. Las defensinas son pequeños péptidos ricos en cisteína con actividad antimicrobiana. Las defensinas de plantas poseen un característico patrón de plegamiento tri-dimensional estabilizado por ocho puentes disulfuro de residuo de cisteinas. Este patrón comparte una alta semejanza con los péptidos de defensa de mamíferos e insectos, sugiriendo un origen común conservado. Funcionalmente estas proteínas exhiben un conjunto diverso de actividades biológicas, aunque todas están al servicio de una función común, como defensoras de sus hospederos. Las defensinas de plantas se activan contra un amplio rango de hongos fitopatogénicos e incluso contra patógenos humanos, lo cual indica su potencial para el desarrollo de terapéuticos. El objetivo de esta revisión es describir brevemente la distribución, función y los modos de actividad antimicrobiana propuestos para las defensinas de plantas, así como reflejar las aplicaciones de las mismas en la agricultura y la medicina. Palabras claves: defensinas, péptidos ricos en cisteína, modo de acción Introduction Plants are constantly exposed to environmental stres- cysteine-rich antifungal peptides ranging from 45 ses and the attacks of pathogenic organisms. Survival to 54 amino acids, and are positively charged. The 1. Ryals JA, Neuenschwander UH, Willits MG, Molina A, Steiner HY, Hunt MD. Sys- under these conditions demands quick defense first plant defensins were isolated from wheat (Tri- temic acquired resistance. Plant Cell 1996; responses to inhibit pathogen spread after initial ticum aestivum) and barley (Hordeum vulgare), and 8:1809-19. infection and thus to limit disease. Among these defense were initially classified as a subgroup of the thionin 2. Kawata M, Nakajima T, Yamamoto T, responses are a rapid oxidative burst, local transcrip- family called the g-thionins since they showed a si- Mori K, Oikawa T, Fukumoto F, Kuroda S. tional activation of defense-related genes, and the milar size and the same number of disulfide bridges as Genetic Engineering for Disease Resistance in Rice (Oryza sativa L.) using antimicrobial generation of yet unknown systemic signals that trigger a and b-thionins [3]. Subsequent identification of Peptides. JARQ 2003;37:71-6. and induce a state of systemic immunity [1]. Small other g-thionin-like proteins in other plant families, 3. Colilla FJ, Rocher R, Mendez E. g-Pu- antimicrobial peptides play an important role as part together with structural information, revealed striking rothionins: amino acid sequence of two of the plants` natural defense system against infectious differences between g-thionins and classical thionins polypeptides of a new family of thionins from wheat endosperm. FEBS Lett 1990; microorganisms, by recognizing a broad range of mi- [4]. This class of proteins was later renamed as “plant 270:191-4. crobes. Hundreds of antifungal peptides and proteins defensins” [5], due to structural and functional simi- are known, with more being discovered almost daily. 4. Terras FRG, Eggermont K, Kovaleva V, larities with insect and mammalian defensins [4]. To Raikhel NV, Osborn RW, Kester A, Ress SB, Genetic engineering has provided a new strategy date, plant defensins have been isolated from seeds Torrekens S, Van Leuven F, Vanderleyden for improving disease resistance through cellular and of various monocot and dicot species or identified by J. Small cysteine-rich antifungal proteins from radish: their role in host defense. Plant molecular tools [2]. Based on in vitro analysis, many the sequencing of cDNA clones. Cell 1995;7:573-88. antimicrobial peptides have inhibited the growth of The plant defensin family is quite diverse regarding 5. Broekaert WF, Terras FRG, Cammue a broad range of plant pathogenic fungi and some amino acid composition as only the eight structure- BPA, Osborn RW. Plant defensins: novel bacteria. The enhancement of disease resistance in stabilizing cysteines appear to be conserved among antimicrobial peptides as components of crops has contributed significantly to increase their the host defense system. Plant Physiol all plant defensins [6]. The variation in the primary 1995;108:1353-8. productivity and decrease the application of sequences may account for the different biological pesticides, which can affect human health and the activities reported for plant defensins. The three- 6. Thomma BPHJ, Thevissen K, Cammue BP. Plants defensins. Planta 2002;216: environment. dimensional structure of plant defensins comprises a 193-202. triple-stranded b-sheet with an a-helix in parallel, Plant defensins 7. Almeida MS, Cabral KM, Kurtenbach E, stabilized by four disulfide bridges [7-8]. This Almeida FC, Valente APJX. Solution structure The main groups of antimicrobial peptides found structure resembles that of insect and mammalian of Pisum sativum defensin 1 by high resolution NMR: plant defensins, identical in plants are thionins, defensins and lipid transfer defensins except that insect defensins lack the domain backbone with different me-chanisms of proteins. Plant defensins are small (c.a. 5kDa), basic, corresponding to the amino-terminal b-strand of plant action. Mol Biol 2002;315:749-57. @ Corresponding author Roxana Portieles et al. Basic insight about plant defensins defensins (Figure 1). Mammalian defensins, on the A B C other hand, not only have a triple-stranded, antiparallel b-sheet, which is roughly comparable in size and spatial orientation to that occurring in plant defensins, but also the a-helix appears to be approximately in the same position relative to the b-sheet [9-10]. The fact that plant defensins, belong to a superfamily of similarly folded antimicrobial peptides that has representati-ves in vertebrates, invertebrates, and plants, suggests that these defense molecules predate the evolutionary divergence of animals and plants. tructure-activity relationships Figure 1. Three-dimensional structure of some known defensins isolated from different organisms. Structures S were downloaded from the protein data bank, PDB accession ID numbers: A. Human b defensin HBD-1 and modes of action (PDB 1E4S) (ref 9). B. Mouse defensin MBD-8 (PDB 1E4R) (ref 9). C. Plant Defensin (PDB 1TI5) (ref 10). The structure-activity relationships and modes of action for most of the plant defensins remain unknown. cation-resistant permeabilization correlates with the Not all plant defensins have the same mode of action. inhibition of fungal growth. Reduction of the antimi- Some of them exhibit potent antifungal activity in crobial activity in the presence of divalent cations, vitro at micromolar concentrations against a broad especially Ca2+, has also been observed for insect and spectrum of filamentous fungi. Morphogenic anti- mammalian defensins [18]. A partial explanation for 8. Fant F, Vranken WF, Borremans FAM. fungal defensins reduce hyphal elongation and induce this effect could be that an increase in ionic strength The three-dimensional solution structure of Aesculus hippocastanum antimicro- hyperbranching, whereas non-morphogenic defensins weakens the electrostatic charge interactions required bial protein 1 determined by 1H nuclear reduce hyphal elongation without causing any mor- for the initial interaction between the peptides and magnetic resonance. Proteins 1999;37: phological distortions [5-11-12]. The plant defensins the membrane. 388-403. Rs-AFP1 and Rs-AFP2 from radish (Raphanus sa- For most plant defensins, molecular components 9. Bauer F, Schweimer K, Kluver E, Cone- tivus), and alfAFP isolated from seeds of the Medicago involved in signaling and putative intracellular targets jo JR, Forssmann WG, Rosch P, Adermann K, Sticht H. Structure determination of sativa (alfalfa) plants [13], are examples of potent an- remain unknown. At present there are two tentative human and murine beta-defensins reveals tifungal proteins, causing morphological distortions models for the mode of action of plant defensins in structural conservation in the absence of significant sequence similarity. Protein Sci of the fungal hyphae, resulting in hyperbranched fungal relation to sphingolipids, that are one of the three major 2001;10:2470-9. structures. The antifungal activity of plant defensins, types of lipids found in eukaryotic membranes, along whether morphogenic or not, is reduced by increasing with sterols
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